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P24664

- TRYP_SACER

UniProt

P24664 - TRYP_SACER

Protein

Trypsin

Gene
N/A
Organism
Saccharopolyspora erythraea (Streptomyces erythraeus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei42 – 421Charge relay system
    Active sitei88 – 881Charge relay system
    Sitei173 – 1731Required for specificityBy similarity
    Active sitei179 – 1791Charge relay system

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.102.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trypsin (EC:3.4.21.4)
    Alternative name(s):
    SET
    OrganismiSaccharopolyspora erythraea (Streptomyces erythraeus)
    Taxonomic identifieri1836 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 227227TrypsinPRO_0000088718Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 43
    Disulfide bondi150 ↔ 164
    Disulfide bondi175 ↔ 199

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    IntActiP24664. 1 interaction.
    MINTiMINT-8289191.

    Structurei

    Secondary structure

    1
    227
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113
    Beta strandi15 – 195
    Beta strandi25 – 339
    Beta strandi36 – 394
    Helixi41 – 444
    Helixi49 – 513
    Beta strandi53 – 575
    Beta strandi66 – 7611
    Helixi83 – 853
    Beta strandi90 – 967
    Helixi111 – 1133
    Beta strandi118 – 12811
    Beta strandi138 – 1447
    Helixi147 – 1537
    Turni159 – 1613
    Beta strandi162 – 1654
    Beta strandi182 – 1854
    Beta strandi188 – 1958
    Beta strandi197 – 2004
    Beta strandi206 – 2105
    Helixi211 – 2144
    Helixi215 – 2228

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4M7GX-ray0.81A1-227[»]
    ProteinModelPortaliP24664.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 223223Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P24664-1 [UniParc]FASTAAdd to Basket

    « Hide

    IVGGEDANVQ DHPFTVALVT PDGQQFCGGT LAAPNKVVTA AHCTVGSQPA    50
    DINVVSGRTV MSSNIGTVSK VTNVWVHPEY QDAAKGFDVS VLTLEAPVKE 100
    APIELAKADD AGYAPDTAAT ILGWGNTSEG GQQADHLQKA TVPVNSDDTC 150
    KQAYGEYTPN AMVCAGVPEG GVDTCQGDSG GPMVVNNKLI GVTSWGEGCA 200
    RPGKPGVYAR VGAYYDVLME QINAGAV 227
    Length:227
    Mass (Da):23,308
    Last modified:March 1, 1992 - v1
    Checksum:iD5AC5E47B227B418
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4M7G X-ray 0.81 A 1-227 [» ]
    ProteinModelPortali P24664.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P24664. 1 interaction.
    MINTi MINT-8289191.

    Protein family/group databases

    MEROPSi S01.102.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Miyamoto K., Matsuo H., Narita K.
      (In) Proceedings of Dai 30 kai tanpakushitsu kouzou touronkai kouen youshishuu, pp.77-80, Tokyo (1979)
      Cited for: PROTEIN SEQUENCE.
    2. "Crystal structure of Streptomyces erythraeus trypsin at 2.7-A resolution."
      Yamane T., Kobuke M., Tsutsui H., Toida T., Suzuki A., Ashida T., Kawata Y., Sakiyama F.
      J. Biochem. 110:945-950(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), SEQUENCE REVISION.

    Entry informationi

    Entry nameiTRYP_SACER
    AccessioniPrimary (citable) accession number: P24664
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Hardly autolyzes itself at all at its active pH range.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3